Conformational stability of calreticulin
Research output: Contribution to journal › Journal article › Research › peer-review
The conformational stability of calreticulin was investigated. Apparent unfolding temperatures (Tm) increased from 31 degrees C at pH 5 to 51 degrees C at pH 9, but electrophoretic analysis revealed that calreticulin oligomerized instead of unfolding. Structural analyses showed that the single C-terminal alpha-helix was of major importance to the conformational stability of calreticulin.
| Original language | English |
|---|---|
| Journal | Protein and Peptide Letters |
| Volume | 12 |
| Issue number | 7 |
| Pages (from-to) | 687-93 |
| Number of pages | 7 |
| ISSN | 0929-8665 |
| Publication status | Published - 2005 |
- Calcium, Calorimetry, Differential Scanning, Calreticulin, Cations, Divalent, Circular Dichroism, Humans, Hydrogen-Ion Concentration, Protein Conformation, Protein Denaturation, Protein Folding, Temperature
Research areas
ID: 40766666